Jonsson P Andreas, Bergemalm Daniel, Andersen Peter M, Gredal Ole, Brännström Thomas, Marklund Stefan L
Department of Medical Biosciences, Clinical Chemistry, Umeå University, Umeå, Sweden.
Ann Neurol. 2008 May;63(5):671-5. doi: 10.1002/ana.21356.
Mutant superoxide dismutases type 1 (SOD1s) cause amyotrophic lateral sclerosis by an unidentified toxic property. In a patient carrying the G127X truncation mutation, minute amounts of SOD1 were found in ventral horns using a mutant-specific antibody. Still, both absolute levels and ratios versus wild-type SOD1 were considerably greater than in other central nervous system areas and peripheral organs. Inclusions of mutant SOD1 were abundant in motoneurons but were also seen in hepatocytes and kidney epithelium. This first examination of mutant SOD1 in both central nervous system and peripheral organs supports the notion that enrichment of misfolded SOD1s might explain the particular vulnerability of motor areas.
突变型1型超氧化物歧化酶（SOD1s）通过一种不明毒性特性导致肌萎缩侧索硬化症。在一名携带G127X截短突变的患者中，使用突变体特异性抗体在腹角发现了微量的SOD1。然而，其绝对水平以及与野生型SOD1的比率均显著高于其他中枢神经系统区域和外周器官。突变型SOD1的包涵体在运动神经元中大量存在，但在肝细胞和肾上皮细胞中也可见到。对中枢神经系统和外周器官中的突变型SOD1进行的首次检查支持了这样一种观点，即错误折叠的SOD1s富集可能解释了运动区域的特殊易损性。
